EC Number   |
General Information |
Reference |
|---|
    2.6.1.14 | physiological function |
Arabidopsis thaliana asparagine aminotransferase (AGT1) is a multifunctional class IV aminotransferase protein that catalyzes transamination reactions using L-serine, L-alanine, and L-asparagine as amino donors and glyoxylate, pyruvate, and hydroxypyruvate as amino acceptors. AGT1 is a peroxisomal aminotransferase with a central role in photorespiration. This enzyme catalyzes various aminotransferase reactions, including serine:glyoxylate, alanine:glyoxylate, and asparagine:glyoxylate transaminations |
759257 |
| 2.6.1.14 | more |
development and evaluation of a method for the prediction of possible genes of orphan enzyme reactions where any associated gene sequences are not determined to date. The candidate enzyme gene of a reaction is detected using the chemical structures of the substrate-product pair (reactant pair). The proposed method is based on a search for similar reactant pairs in a reference database (KEGG database) and offers orthologeous groups that possibly mediate the given reaction. One example is the asparagine oxo-acid transaminase (R01346, EC 2.6.1.14), which transfers an amino group from asparagine to glutamate, the paralogue reactant pair is the asparagine-oxaloacetamide pair correlated to gene SMU_24 (UniProt ID Q8DWM1) |
-, 759546 |
| 2.6.1.14 | more |
in the enzyme crystal, another dimer related by noncrystallographic symmetry makes close interactions to form a tetramer mediated in part by an extra carboxyl-terminal helix conserved in plant homologues of AGT1. Residues Tyr35' and Arg36', entering the active site from the other subunits in the dimer, mediate interactions between AGT and L-serine when used as a substrate. Structural model of AGT1 and structure-function analysis, structure comparisons, detailed overview |
759257 |
